Abstract:
:High-mobility group box-1 (HMGB1) is remarkably mobile in living cells, which reflects its ability to interact only transiently with both DNA and protein. This property is likely essential for HMGB1 nuclear activities. Nonetheless the weak interaction of HMGB1 with DNA and/or protein partners has also been a major limitation for investigating HMGB1 subnuclear localisation and for the identification of HMGB1 containing complexes by conventional biochemical approaches. In the present study, FRAP experiments demonstrated that DsRed-mediated oligomerization strongly reduces HMGB1 mobility due to an increased affinity for cellular chromatin. Moreover, oligomerized DsRed-HMGB1 exhibited a higher affinity for supercoiled DNA in vitro compared to its monomeric counterpart. These results indicate that DsRed-meditated oligomerization is prone to stabilize labile interactions involving HMGB1 both in vivo and in vitro.
journal_name
Biochimiejournal_title
Biochimieauthors
Messmer M,Klein C,Boniface R,Gnädig NF,Lecerf M,Barnay-Verdier S,Maréchal Vdoi
10.1016/j.biochi.2012.11.001subject
Has Abstractpub_date
2013-04-01 00:00:00pages
962-6issue
4eissn
0300-9084issn
1638-6183pii
S0300-9084(12)00444-0journal_volume
95pub_type
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